Human Poly A Binding Protein Nuclear 1 (PABPN1) interaction partners

we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding proteinPABPN1 and the poly(A)-specific RNase PARN (show PARN Antibodies).

Many ribozymes were assayed and validated, including four ribozymes targeting the transcript of a disease-causing gene (a mutant version of PABPN1).

Studied if the stability of the RNP (show RNPC3 Antibodies) domain of PABPN1 or domain swapping within the RNP (show RNPC3 Antibodies) domain may add to fibril formation.

This function is mediated by the concerted actions of the nuclear poly(A) binding proteinPABPN1, poly(A) polymerase (PAP (show PAPOLA Antibodies)), and the nuclear exosome complex, a pathway we have named PABPN1 and PAP (show REG3A Antibodies)-mediated RNA decay (PPD (show HPD Antibodies))

These findings demonstrate a role for PABPN1 in rescuing several cytopathological features of TDP-43 (show TARDBP Antibodies) proteinopathy by increasing the turnover of pathologic proteins.

PABPN1 inhibits expression of transcripts with pAs (show PASK Antibodies) near the transcription start site (TSS (show RPL38 Antibodies)), a property possibly related to its role in RNA degradation

the first step of the cleavage and polyadenylation reaction, mRNA cleavage, is affected in muscles expressing alanine-expanded PABPN1. We propose that impaired cleavage is an early defect in Oculopharyngeal muscular dystrophy.

These findings demonstrate a role for PABPN1 in rescuing several cytopathological features of TDP-43 (show TARDBP Antibodies) proteinopathy by increasing the turnover of pathologic proteins.

the first step of the cleavage and polyadenylation reaction, mRNA cleavage, is affected in muscles expressing alanine-expanded PABPN1. We propose that impaired cleavage is an early defect in Oculopharyngeal muscular dystrophy.

PAB2 was partially retargeted to the nucleolus in the presence of TuMV VPg-Pro. In addition, the membrane association of PAB2 during TuMV infection resulted from the internalization of the host protein in 6K-VPg-Pro-induced vesicles.

Thus, Hsc70-3 and PABP2 are potentially integral components of the replicase complex and could have important roles to play in the regulation of potyviral RdRp functions.

Poly A Binding Protein Nuclear 1 (PABPN1) Antigen Profile

Protein Summary

This gene encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. The protein is required for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and controls the size of the poly(A) tail to about 250 nt. At steady-state, this protein is localized in the nucleus whereas a different poly(A) binding protein is localized in the cytoplasm. This gene contains a GCG trinucleotide repeat at the 5' end of the coding region, and expansion of this repeat from the normal 6 copies to 8-13 copies leads to autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Related pseudogenes have been identified on chromosomes 19 and X. Read-through transcription also exists between this gene and the neighboring upstream BCL2-like 2 (BCL2L2) gene.